The metal-dependent enzymes collagenase (MMP-I and MMP-8), gelatinase/- Type IV collagenase (MMP-2), and stromelysin (MMP-3) are members of the class of neutral matrix metalloproteinases which degrade connective tissue elements of tissues such as bone, cartilage, skin and basement membrane. The natural substrates for these enzymes include both helical and/or denatured collagens, proteoglycans, and other matrix proteins. In view of the ubiquitous distribution of these substrates, it is not surprising that these dental disease, diabetes, ophthalmologic conditions, neoplasia, metabolic bone disease, and orthopaedic conditions. Identification of agents which might inhibit collagenase and other MMPs has long seemed a reasonable therapeutic goal for modulation of connective tissue degradation. In view of the wide range of potential applications for MMP inhibitors, and the diversity of theoretically useful agents, a multidisciplinary conference to discuss mechanisms of action and models for drug development would contribute substantially to progress in the field. A preliminary schedule has been assembled which includes workers in biochemistry, molecular biology, dentistry, rheumatology, oncology, ophthalmology, and pathology. The scope of the conference will extend from regulation of synthesis and/or activity to exchange of ideas about the design of clinical trials in various disease states, plus detailed of discussion of mechanism of action of MMP inhibitors.